CD244_RAT
ID CD244_RAT Reviewed; 311 AA.
AC Q9JLM2; Q9JLM3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Natural killer cell receptor 2B4;
DE AltName: Full=NK cell type I receptor protein 2B4;
DE Short=NKR2B4;
DE AltName: Full=Non-MHC restricted killing associated;
DE AltName: CD_antigen=CD244;
DE Flags: Precursor;
GN Name=Cd244; Synonyms=2b4, Nmrk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10803843; DOI=10.1007/s002510050624;
RA Kumaresan P.R., Stepp S.E., Bennett M., Kumar V., Mathew P.A.;
RT "Molecular cloning of transmembrane and soluble forms of a novel rat
RT natural killer cell receptor related to 2B4.";
RL Immunogenetics 51:306-313(2000).
CC -!- FUNCTION: Modulate other receptor-ligand interactions to enhance
CC leukocyte activation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CD48. Following phosphorylation, it is able to
CC recruit PTPN11/SHP-2 and SH2D1A/SAP. Binding of SH2D1A/SAP to CD244
CC prevents its association with PTPN11/SHP-2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; AF156988; AAF71161.1; -; mRNA.
DR EMBL; AF156989; AAF71162.1; -; mRNA.
DR RefSeq; NP_071595.1; NM_022259.1.
DR AlphaFoldDB; Q9JLM2; -.
DR SMR; Q9JLM2; -.
DR STRING; 10116.ENSRNOP00000006266; -.
DR GlyGen; Q9JLM2; 6 sites.
DR PaxDb; Q9JLM2; -.
DR GeneID; 64025; -.
DR KEGG; rno:64025; -.
DR UCSC; RGD:68400; rat.
DR CTD; 51744; -.
DR RGD; 68400; Cd244.
DR eggNOG; ENOG502S7N7; Eukaryota.
DR InParanoid; Q9JLM2; -.
DR PhylomeDB; Q9JLM2; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:Q9JLM2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001773; P:myeloid dendritic cell activation; ISO:RGD.
DR GO; GO:0002323; P:natural killer cell activation involved in immune response; ISO:RGD.
DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; ISO:RGD.
DR GO; GO:0071663; P:positive regulation of granzyme B production; ISO:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024304; NK_rcpt_2B4.
DR InterPro; IPR024303; NK_rcpt_2B4_Ig_dom.
DR PANTHER; PTHR12080:SF56; PTHR12080:SF56; 1.
DR Pfam; PF11465; Receptor_2B4; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..311
FT /note="Natural killer cell receptor 2B4"
FT /id="PRO_0000014670"
FT TOPO_DOM 20..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..128
FT /note="Ig-like 1"
FT DOMAIN 131..215
FT /note="Ig-like 2"
FT REGION 275..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..118
FT /evidence="ECO:0000250"
FT DISULFID 153..195
FT /evidence="ECO:0000255"
FT CONFLICT 46
FT /note="A -> T (in Ref. 1; AAF71161)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..204
FT /note="YGTHWENRTDASSLHTYTCNVSNKASWA -> IQLSALCGIHRYPRQIFSWG
FT HRLLLCVE (in Ref. 1; AAF71161)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..311
FT /note="Missing (in Ref. 1; AAF71161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35300 MW; 5A527D22D2565772 CRC64;
MLQQTVLLSL FLLLRAHQGQ DCADSSEEVL GVSGKPVRLR PSNIQAKHVS IEWKKKTGHQ
QTPQIVTWDT TDNKNFNMCC SDIYGFESEN FALSIKSAKL NDSGHYLLEI TNQRGIVCTK
NFQMLIFDPV ETPHLTVQGT LWANGTCQLS LSCFVPKDDN VSYALYRGSM LISNQRYGTH
WENRTDASSL HTYTCNVSNK ASWANHTLTS PQSCQSVPSK FNYLPFMVSI GILVKFFHGA
IDCFCVWNRK RKQSQSIAKE SLTIHEYVKN AQVSRDQRGH FRASGSSSDV RGDERGQRES
DRRLFQFINR S
